MAPK MODULES

3D organization of yeast MAP-kinase modules

Coordinatore	EOTVOS LORAND TUDOMANYEGYETEM    more  Organization address address: EGYETEM TER 1-3 city: BUDAPEST postcode: 1053 contact info Titolo: Prof. Nome: Ferenc Cognome: Hudecz Email: send email Telefono: -2663084 Fax: -10017
Nazionalità Coordinatore	Hungary [HU]
Totale costo	100˙000 €
EC contributo	100˙000 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2007-4-3-IRG
Funding Scheme	MC-IRG
Anno di inizio	2008
Periodo (anno-mese-giorno)	2008-04-01   -   2012-03-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	EOTVOS LORAND TUDOMANYEGYETEM  Organization address address: EGYETEM TER 1-3 city: BUDAPEST postcode: 1053 contact info Titolo: Prof. Nome: Ferenc Cognome: Hudecz Email: send email Telefono: -2663084 Fax: -10017	HU (BUDAPEST)	coordinator	0.00

Mappa

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 Obiettivo del progetto (Objective)

'Eukaryotic cells contain myriad signaling pathways used to transmit information from the plasma membrane to the nucleus. Given the large number of pathways in a cell, how is it that a given stimulus leads to a precise response? This problem is particularly acute in kinase pathways, such as mitogen-activated protein kinase (MAPK) cascades, which often share common protein components. Over the last decade, however, a paradigm that has emerged is that signaling pathway specificity can be mediated, in part, by scaffolding proteins that bind pathway members and restrict them to act only on one another. In yeast, as well as in mammals, several scaffold proteins for MAP-kinase cascades have been identified. These scaffolds allow one or more common kinases to function in distinct signaling pathways without improper cross-talk. However, very little is known about the mechanism by which these scaffold molecules physically control transmission of signaling information. We therefore plan to determine the three-dimensional structures of MAP-kinase modules of the yeast mating and high osmolarity response pathways, which are organized by two non-related scaffold proteins: Ste5 and Pbs2. The components (four kinases and two scaffold proteins) will be expressed as recombinant proteins and the complex reconstituted in vitro. We will use a multifaceted approach with the following specific aims: (1) to determine the structure of the reconstituted Ste5 and Pbs2 scaffolded complex by X-ray crystallography or electron cryomicroscopy and (2) to identify well-ordered fragments of the scaffolds that interact with individual member kinases to determine the structure of informative sub-complexes by X-ray crystallography.'

Introduzione (Teaser)

Signals exchanged between cells on a microscopic level shed light on intricate biological systems. The results could help to understand disease and develop treatments.